Bulletin of the Chemical Society of Japan p. 125 - 133 (1984)
Update date:2022-08-04
Topics:
Yoshimura
Miki
Ikemura
Aimoto
Shimonishi
Takeda
Takeda
Miwatani
Two peptides with the two primary structures of 18 amino acid residues proposed for a heat-stable enterotoxin from enterotoxigenic Escherichia coli strain 18D were synthesized by solution methods and their physicochemical and biological properties were compared with those of native toxin. One of these peptides Asn-Thr-Phe-Tyr-Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Ala-Gly-Cys- Tyr) showed the same heat-stability and **1H-NMR spectrum as those of the native toxin and evoked fluid secretion in suckling mice at a dose of 1. 5-2. 0 ng, which is similar to the effective dose of native toxin. Moreover, its toxicity was neutralized by antisera against the native toxin.
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